HEADER IMMUNE SYSTEM 05-DEC-24 9MDZ TITLE ANTI-IL23R VHH COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-IL23R VHH; COMPND 3 CHAIN: E; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_TAXID: 9844; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: CHO KEYWDS IBD, INFLAMMATORY BOWEL DISEASE, INFLAMMATION, IMMUNOLOGY, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.R.KIEFER,J.T.KOERBER,N.OTA,C.DAVIES,H.A.WALLWEBER REVDAT 1 21-MAY-25 9MDZ 0 JRNL AUTH N.OTA,C.DAVIES,H.A.WALLWEBER,J.R.KIEFER,J.T.KOERBER JRNL TITL ORAL SINGLE DOMAIN ANTIBODY INHIBITION OF IL-23 SIGNALING JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.27 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.27 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.72 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 42297 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.145 REMARK 3 R VALUE (WORKING SET) : 0.145 REMARK 3 FREE R VALUE : 0.159 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950 REMARK 3 FREE R VALUE TEST SET COUNT : 2092 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 39.7200 - 3.1400 1.00 2972 133 0.1451 0.1600 REMARK 3 2 3.1400 - 2.5000 1.00 2811 152 0.1460 0.1556 REMARK 3 3 2.5000 - 2.1800 1.00 2790 132 0.1328 0.1417 REMARK 3 4 2.1800 - 1.9800 1.00 2756 146 0.1250 0.1421 REMARK 3 5 1.9800 - 1.8400 1.00 2783 138 0.1315 0.1567 REMARK 3 6 1.8400 - 1.7300 1.00 2728 151 0.1485 0.1376 REMARK 3 7 1.7300 - 1.6400 1.00 2732 147 0.1406 0.1428 REMARK 3 8 1.6400 - 1.5700 1.00 2722 148 0.1361 0.1689 REMARK 3 9 1.5700 - 1.5100 1.00 2752 143 0.1438 0.1846 REMARK 3 10 1.5100 - 1.4600 1.00 2712 155 0.1611 0.1909 REMARK 3 11 1.4600 - 1.4100 1.00 2722 144 0.1741 0.1907 REMARK 3 12 1.4100 - 1.3700 1.00 2716 135 0.1658 0.1645 REMARK 3 13 1.3700 - 1.3400 0.98 2664 130 0.1747 0.2218 REMARK 3 14 1.3400 - 1.3000 0.91 2458 138 0.1956 0.1990 REMARK 3 15 1.3000 - 1.2700 0.69 1887 100 0.2776 0.3213 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.120 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.310 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.006 NULL REMARK 3 ANGLE : 0.883 NULL REMARK 3 CHIRALITY : 0.076 145 REMARK 3 PLANARITY : 0.023 187 REMARK 3 DIHEDRAL : 18.824 367 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.8208 35.6167 9.7150 REMARK 3 T TENSOR REMARK 3 T11: 0.1810 T22: 0.2076 REMARK 3 T33: 0.1157 T12: 0.0233 REMARK 3 T13: -0.0027 T23: 0.0125 REMARK 3 L TENSOR REMARK 3 L11: 0.5165 L22: 0.8360 REMARK 3 L33: 0.0267 L12: 0.2488 REMARK 3 L13: 0.1023 L23: 0.1055 REMARK 3 S TENSOR REMARK 3 S11: -0.0265 S12: -0.6208 S13: 0.0052 REMARK 3 S21: 0.5503 S22: 0.0355 S23: 0.0676 REMARK 3 S31: -0.0562 S32: -0.7597 S33: -0.0114 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 8 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.6346 30.8317 -13.5068 REMARK 3 T TENSOR REMARK 3 T11: 0.1225 T22: 0.1749 REMARK 3 T33: 0.1119 T12: -0.0119 REMARK 3 T13: -0.0307 T23: 0.0080 REMARK 3 L TENSOR REMARK 3 L11: 0.0245 L22: 0.2702 REMARK 3 L33: 0.7478 L12: 0.0405 REMARK 3 L13: 0.0234 L23: -0.1662 REMARK 3 S TENSOR REMARK 3 S11: -0.0620 S12: 0.0676 S13: 0.0773 REMARK 3 S21: -0.1642 S22: 0.0430 S23: 0.1808 REMARK 3 S31: -0.1393 S32: -0.2889 S33: 0.0365 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 18 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.8530 40.3400 5.3316 REMARK 3 T TENSOR REMARK 3 T11: 0.1198 T22: 0.1215 REMARK 3 T33: 0.1255 T12: 0.0092 REMARK 3 T13: -0.0066 T23: -0.0145 REMARK 3 L TENSOR REMARK 3 L11: 0.5257 L22: 0.2161 REMARK 3 L33: 0.3316 L12: -0.1790 REMARK 3 L13: -0.4175 L23: 0.1336 REMARK 3 S TENSOR REMARK 3 S11: 0.0131 S12: -0.1214 S13: 0.1444 REMARK 3 S21: -0.0263 S22: 0.0668 S23: -0.0007 REMARK 3 S31: -0.0808 S32: -0.0269 S33: 0.0001 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 33 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.2048 31.1120 0.2755 REMARK 3 T TENSOR REMARK 3 T11: 0.0929 T22: 0.1120 REMARK 3 T33: 0.1029 T12: -0.0032 REMARK 3 T13: 0.0011 T23: 0.0014 REMARK 3 L TENSOR REMARK 3 L11: 0.3170 L22: 0.1151 REMARK 3 L33: 0.2256 L12: -0.0350 REMARK 3 L13: -0.0104 L23: -0.1340 REMARK 3 S TENSOR REMARK 3 S11: 0.0720 S12: -0.0592 S13: -0.0288 REMARK 3 S21: 0.0784 S22: -0.0183 S23: -0.0612 REMARK 3 S31: 0.0619 S32: 0.0145 S33: -0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 40 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.6439 25.4718 -1.4388 REMARK 3 T TENSOR REMARK 3 T11: 0.1197 T22: 0.1137 REMARK 3 T33: 0.1742 T12: -0.0053 REMARK 3 T13: -0.0187 T23: 0.0071 REMARK 3 L TENSOR REMARK 3 L11: 0.8446 L22: 0.0550 REMARK 3 L33: 0.4641 L12: 0.0271 REMARK 3 L13: 0.0443 L23: 0.0232 REMARK 3 S TENSOR REMARK 3 S11: 0.0917 S12: -0.0068 S13: -0.3668 REMARK 3 S21: 0.1295 S22: -0.0562 S23: -0.2466 REMARK 3 S31: 0.1180 S32: -0.0248 S33: -0.0001 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 52 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.0987 38.0152 -5.4671 REMARK 3 T TENSOR REMARK 3 T11: 0.0957 T22: 0.1320 REMARK 3 T33: 0.1230 T12: 0.0071 REMARK 3 T13: 0.0043 T23: 0.0061 REMARK 3 L TENSOR REMARK 3 L11: 0.8610 L22: 0.5266 REMARK 3 L33: 0.5535 L12: 0.3432 REMARK 3 L13: 0.0053 L23: -0.4313 REMARK 3 S TENSOR REMARK 3 S11: 0.0224 S12: 0.1560 S13: 0.1241 REMARK 3 S21: -0.0402 S22: 0.0397 S23: -0.0527 REMARK 3 S31: -0.0827 S32: -0.0432 S33: 0.0026 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 73 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.5064 41.7916 -1.7118 REMARK 3 T TENSOR REMARK 3 T11: 0.1107 T22: 0.1253 REMARK 3 T33: 0.1320 T12: 0.0116 REMARK 3 T13: 0.0031 T23: 0.0069 REMARK 3 L TENSOR REMARK 3 L11: 0.1939 L22: 0.2150 REMARK 3 L33: 0.4877 L12: 0.1884 REMARK 3 L13: -0.3115 L23: -0.3000 REMARK 3 S TENSOR REMARK 3 S11: 0.0744 S12: 0.0313 S13: 0.1132 REMARK 3 S21: 0.0595 S22: 0.0676 S23: 0.0284 REMARK 3 S31: -0.0804 S32: -0.1093 S33: 0.0009 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 83 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.7039 29.1883 -5.3251 REMARK 3 T TENSOR REMARK 3 T11: 0.1083 T22: 0.1260 REMARK 3 T33: 0.1010 T12: -0.0134 REMARK 3 T13: 0.0050 T23: -0.0002 REMARK 3 L TENSOR REMARK 3 L11: 0.9254 L22: 0.5099 REMARK 3 L33: 0.2353 L12: -0.0395 REMARK 3 L13: 0.3759 L23: -0.1775 REMARK 3 S TENSOR REMARK 3 S11: -0.0351 S12: 0.1191 S13: 0.0038 REMARK 3 S21: -0.0715 S22: 0.0156 S23: -0.0103 REMARK 3 S31: 0.0482 S32: 0.0952 S33: 0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 99 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.9093 31.9348 9.0142 REMARK 3 T TENSOR REMARK 3 T11: 0.1187 T22: 0.1855 REMARK 3 T33: 0.1302 T12: -0.0037 REMARK 3 T13: -0.0060 T23: 0.0086 REMARK 3 L TENSOR REMARK 3 L11: 0.3797 L22: 0.3589 REMARK 3 L33: 0.5389 L12: 0.0653 REMARK 3 L13: 0.0823 L23: -0.2080 REMARK 3 S TENSOR REMARK 3 S11: 0.0411 S12: -0.3696 S13: -0.0490 REMARK 3 S21: 0.0473 S22: -0.0979 S23: -0.1248 REMARK 3 S31: 0.0597 S32: 0.1127 S33: -0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 114 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.5318 25.6394 -10.2465 REMARK 3 T TENSOR REMARK 3 T11: 0.1529 T22: 0.1595 REMARK 3 T33: 0.1083 T12: -0.0387 REMARK 3 T13: -0.0228 T23: -0.0060 REMARK 3 L TENSOR REMARK 3 L11: 0.2151 L22: 0.3834 REMARK 3 L33: 0.3494 L12: -0.0460 REMARK 3 L13: -0.1708 L23: 0.0632 REMARK 3 S TENSOR REMARK 3 S11: -0.1963 S12: 0.1515 S13: 0.0014 REMARK 3 S21: -0.3076 S22: 0.0620 S23: 0.1742 REMARK 3 S31: -0.0967 S32: -0.2238 S33: -0.0111 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9MDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290795. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-SEP-22 REMARK 200 TEMPERATURE (KELVIN) : 103 REMARK 200 PH : 7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00005 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42302 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.270 REMARK 200 RESOLUTION RANGE LOW (A) : 44.410 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 200 DATA REDUNDANCY : 10.80 REMARK 200 R MERGE (I) : 0.03700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 29.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.27 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.30 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.33200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 800 MM SODIUM SUCCINATE, PH 7, VAPOR REMARK 280 DIFFUSION, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 -X,Y,-Z REMARK 290 6555 X,-Y,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 62.80750 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 62.80750 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 20.78150 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 62.80750 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 62.80750 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 20.78150 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 62.80750 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 62.80750 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 20.78150 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 62.80750 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 62.80750 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 20.78150 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 62.80750 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 62.80750 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 20.78150 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 62.80750 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 62.80750 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 20.78150 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 62.80750 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 62.80750 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 20.78150 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 62.80750 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 62.80750 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 20.78150 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH E 331 LIES ON A SPECIAL POSITION. REMARK 375 HOH E 378 LIES ON A SPECIAL POSITION. REMARK 375 HOH E 436 LIES ON A SPECIAL POSITION. REMARK 375 HOH E 476 LIES ON A SPECIAL POSITION. REMARK 375 HOH E 516 LIES ON A SPECIAL POSITION. REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG E 45 0.18 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH E 525 DISTANCE = 6.30 ANGSTROMS REMARK 525 HOH E 526 DISTANCE = 10.05 ANGSTROMS DBREF 9MDZ E 1 120 PDB 9MDZ 9MDZ 1 120 SEQRES 1 E 120 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 120 PHE THR PHE SER THR TYR ALA MET ALA TRP PHE ARG GLN SEQRES 4 E 120 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLU SER TRP SEQRES 5 E 120 SER SER GLY THR THR TYR TYR GLY ALA SER VAL VAL GLY SEQRES 6 E 120 ARG PHE THR MET SER ARG ASP ASP SER LYS ASN THR VAL SEQRES 7 E 120 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 E 120 VAL TYR TYR CYS ALA ALA LYS ARG PRO ASP ALA GLY TRP SEQRES 9 E 120 GLN THR TYR ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 E 120 VAL SER SER HET GOL E 201 14 HET GOL E 202 14 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 GOL 2(C3 H8 O3) FORMUL 4 HOH *226(H2 O) HELIX 1 AA1 THR E 28 TYR E 32 5 5 HELIX 2 AA2 ARG E 86 THR E 90 5 5 SHEET 1 AA1 4 GLN E 3 SER E 7 0 SHEET 2 AA1 4 LEU E 18 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AA1 4 THR E 77 MET E 82 -1 O MET E 82 N LEU E 18 SHEET 4 AA1 4 PHE E 67 ASP E 72 -1 N THR E 68 O GLN E 81 SHEET 1 AA2 6 GLY E 10 VAL E 12 0 SHEET 2 AA2 6 THR E 114 VAL E 118 1 O THR E 117 N VAL E 12 SHEET 3 AA2 6 ALA E 91 LYS E 98 -1 N TYR E 93 O THR E 114 SHEET 4 AA2 6 ALA E 33 GLN E 39 -1 N PHE E 37 O TYR E 94 SHEET 5 AA2 6 GLU E 46 SER E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AA2 6 THR E 57 TYR E 59 -1 O TYR E 58 N GLU E 50 SHEET 1 AA3 4 GLY E 10 VAL E 12 0 SHEET 2 AA3 4 THR E 114 VAL E 118 1 O THR E 117 N VAL E 12 SHEET 3 AA3 4 ALA E 91 LYS E 98 -1 N TYR E 93 O THR E 114 SHEET 4 AA3 4 TYR E 109 TRP E 110 -1 O TYR E 109 N ALA E 97 SSBOND 1 CYS E 22 CYS E 95 1555 1555 2.03 CRYST1 125.615 125.615 41.563 90.00 90.00 90.00 I 4 2 2 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.007961 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007961 0.000000 0.00000 SCALE3 0.000000 0.000000 0.024060 0.00000